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Crystal structure of MIRANDA/STAUFEN DSRBD5 complex

Analyse Crystal structure of MIRANDA/STAUFEN DSRBD5 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5CFF
Type
protein
Length
626 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Miranda; Staufen
UniProt
Q9VDR7, P25159
Pockets
1 · best druggability 0.29

Structure

x-ray diffraction · 7 distinct chains · 77% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMirandaprotein8798% helix, 0% strandQ9VDR7
BMirandaprotein8898% helix, 0% strandQ9VDR7
CMirandaprotein8795% helix, 0% strandQ9VDR7
DMirandaprotein8897% helix, 0% strandQ9VDR7
E, GStaufenprotein7041% helix, 29% strandP25159
FStaufenprotein7142% helix, 28% strandP25159
HStaufenprotein6546% helix, 31% strandP25159

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1740.290.7313empty

Interfaces

12 interfaces between chains.

  • B–D · 2334 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 2221 Ų buried · 7 hydrogen bonds · protein-protein
  • B–E · 745 Ų buried · 6 hydrogen bonds · protein-protein
  • D–G · 741 Ų buried · 9 hydrogen bonds · protein-protein
  • A–F · 730 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 5CFF · Crystal structure of Miranda/Staufen dsRBD5 complex · the same entry in another collection · chain H against H, TM-score 1.00
  • P25159 · AlphaFold monomer V2.0 prediction for maternal effect protein staufen (P25159) · a predicted model of the same protein · chain H against A, TM-score 0.97

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